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Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome
BACKGROUND: Amyloidosis leads to deposition of abnormal protein with beta-pleated sheet structure in specific compartments of the affected organs. The histological localization of these amyloid deposits determines the overall survival of the patient. METHODS: In this study we have assessed the histo...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4424547/ https://www.ncbi.nlm.nih.gov/pubmed/25924613 http://dx.doi.org/10.1186/s12882-015-0046-0 |
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author | Castano, Ekaterina Palmer, Matthew B Vigneault, Christine Luciano, Randy Wong, Serena Moeckel, Gilbert |
author_facet | Castano, Ekaterina Palmer, Matthew B Vigneault, Christine Luciano, Randy Wong, Serena Moeckel, Gilbert |
author_sort | Castano, Ekaterina |
collection | PubMed |
description | BACKGROUND: Amyloidosis leads to deposition of abnormal protein with beta-pleated sheet structure in specific compartments of the affected organs. The histological localization of these amyloid deposits determines the overall survival of the patient. METHODS: In this study we have assessed the histological localization and severity of amyloid deposition in 35 patients with biopsy-proven renal amyloidosis and have compared those to clinical parameters, histo-pathological injury criteria and respective patient outcome. Comparisons were statistically analyzed using thus comparison between the different study groups, which was done using Student t-test and analysis of variance. RESULTS: We find that the glomerulus is by far the most commonly and most severely affected renal compartment and patients with severe glomerular amyloidosis advance faster towards end stage renal disease (ESRD) and death, compared to those patients without glomerular amyloid deposits. Patients with severe glomerular amyloidosis showed higher serum creatinine and urine protein levels, while patients with severe vascular amyloidosis showed higher levels of interstitial inflammatory infiltrate. CONCLUSION: In kidneys affected by amyloidosis, the amyloid proteins are predominantly deposited along vessels, especially the small vessels including glomerular capillary loops. The severity of glomerular amyloid deposition enhances the risk of developing ESRD and increases the risk for premature death. |
format | Online Article Text |
id | pubmed-4424547 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-44245472015-05-09 Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome Castano, Ekaterina Palmer, Matthew B Vigneault, Christine Luciano, Randy Wong, Serena Moeckel, Gilbert BMC Nephrol Research Article BACKGROUND: Amyloidosis leads to deposition of abnormal protein with beta-pleated sheet structure in specific compartments of the affected organs. The histological localization of these amyloid deposits determines the overall survival of the patient. METHODS: In this study we have assessed the histological localization and severity of amyloid deposition in 35 patients with biopsy-proven renal amyloidosis and have compared those to clinical parameters, histo-pathological injury criteria and respective patient outcome. Comparisons were statistically analyzed using thus comparison between the different study groups, which was done using Student t-test and analysis of variance. RESULTS: We find that the glomerulus is by far the most commonly and most severely affected renal compartment and patients with severe glomerular amyloidosis advance faster towards end stage renal disease (ESRD) and death, compared to those patients without glomerular amyloid deposits. Patients with severe glomerular amyloidosis showed higher serum creatinine and urine protein levels, while patients with severe vascular amyloidosis showed higher levels of interstitial inflammatory infiltrate. CONCLUSION: In kidneys affected by amyloidosis, the amyloid proteins are predominantly deposited along vessels, especially the small vessels including glomerular capillary loops. The severity of glomerular amyloid deposition enhances the risk of developing ESRD and increases the risk for premature death. BioMed Central 2015-04-29 /pmc/articles/PMC4424547/ /pubmed/25924613 http://dx.doi.org/10.1186/s12882-015-0046-0 Text en © Castano et al.; licensee BioMed Central. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Castano, Ekaterina Palmer, Matthew B Vigneault, Christine Luciano, Randy Wong, Serena Moeckel, Gilbert Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome |
title | Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome |
title_full | Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome |
title_fullStr | Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome |
title_full_unstemmed | Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome |
title_short | Comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome |
title_sort | comparison of amyloid deposition in human kidney biopsies as predictor of poor patient outcome |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4424547/ https://www.ncbi.nlm.nih.gov/pubmed/25924613 http://dx.doi.org/10.1186/s12882-015-0046-0 |
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